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Protein

Ligninase LG6

Gene

GLG6

Organism
Phanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Depolymerization of lignin. Catalyzes the C(alpha)-C(beta) cleavage of the propyl side chains of lignin.

Catalytic activityi

1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 3,4-dimethoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O.
2 (3,4-dimethoxyphenyl)methanol + H2O2 = 2 (3,4-dimethoxyphenyl)methanol radical + 2 H2O.

Cofactori

Protein has several cofactor binding sites:
  • heme bPROSITE-ProRule annotationNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.PROSITE-ProRule annotation
  • Ca2+PROSITE-ProRule annotationNote: Binds 2 calcium ions per subunit.PROSITE-ProRule annotation

Pathwayi: lignin degradation

This protein is involved in the pathway lignin degradation, which is part of Secondary metabolite metabolism.
View all proteins of this organism that are known to be involved in the pathway lignin degradation and in Secondary metabolite metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei71 – 711Transition state stabilizerPROSITE-ProRule annotation
Active sitei75 – 751Proton acceptorPROSITE-ProRule annotation
Metal bindingi76 – 761Calcium 1PROSITE-ProRule annotation
Metal bindingi94 – 941Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi96 – 961Calcium 1PROSITE-ProRule annotation
Metal bindingi98 – 981Calcium 1PROSITE-ProRule annotation
Metal bindingi204 – 2041Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi205 – 2051Calcium 2PROSITE-ProRule annotation
Metal bindingi222 – 2221Calcium 2PROSITE-ProRule annotation
Metal bindingi224 – 2241Calcium 2PROSITE-ProRule annotation
Metal bindingi227 – 2271Calcium 2; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi229 – 2291Calcium 2PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide, Lignin degradation

Keywords - Ligandi

Calcium, Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14342.
UniPathwayiUPA00892.

Protein family/group databases

CAZyiAA2. Auxiliary Activities 2.
PeroxiBasei2415. PcLiP06.

Names & Taxonomyi

Protein namesi
Recommended name:
Ligninase LG6 (EC:1.11.1.14)
Alternative name(s):
Diarylpropane peroxidase
Lignin peroxidase
Gene namesi
Name:GLG6
OrganismiPhanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Taxonomic identifieri5306 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesPhanerochaetaceaePhanerochaete

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Propeptidei22 – 287Sequence analysisPRO_0000023770
Chaini29 – 372344Ligninase LG6PRO_0000023771Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi31 ↔ 43PROSITE-ProRule annotation
Disulfide bondi62 ↔ 148PROSITE-ProRule annotation
Disulfide bondi277 ↔ 345PROSITE-ProRule annotation
Glycosylationi285 – 2851N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

Structurei

3D structure databases

ProteinModelPortaliP50622.
SMRiP50622. Positions 24-372.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peroxidase family. Ligninase subfamily.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410II1B. Eukaryota.
ENOG410ZS1R. LUCA.

Family and domain databases

InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR001621. Ligninase.
IPR024589. Ligninase_C.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF11895. DUF3415. 1 hit.
PF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00462. LIGNINASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P50622-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALKQLAAAV ALALSIQAAQ GAAVKEKRAT CSNGATVGDA SSCAWFDVLD
60 70 80 90 100
DIQQNLFNGA QCGAEAHESI RLVFHDAIAI SPALESQGKF GGGGADGSII
110 120 130 140 150
LFDDIETNFH PNIGLDEIVN LQKPFIQKHG VTPGDFIAFA GAVAMSNCPG
160 170 180 190 200
APQMNFFTGR APATQAAPDG LVPEPFHTVD QIISRVNDAG EFDELELVWM
210 220 230 240 250
LSAHSVAAAN DVDPTIQGLA FDSTPGVFDS QFFVETQLRG TAFPGSGGNQ
260 270 280 290 300
GEVESPLPGE MRLQSDSSIA RDSRTACEWQ SFVNNQSKLV SDFQFIFLAL
310 320 330 340 350
TQLGENPDAM TDCSDVIPIS KPVPNNVPFS FFPAGKTMAD VEQACAETPF
360 370
PTLTTLPGPE TSVQRIQPPP GA
Length:372
Mass (Da):39,259
Last modified:October 1, 1996 - v1
Checksum:iB192A93351F8CC16
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80213 mRNA. Translation: AAA33737.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80213 mRNA. Translation: AAA33737.1.

3D structure databases

ProteinModelPortaliP50622.
SMRiP50622. Positions 24-372.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiAA2. Auxiliary Activities 2.
PeroxiBasei2415. PcLiP06.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410II1B. Eukaryota.
ENOG410ZS1R. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00892.
BioCyciMetaCyc:MONOMER-14342.

Family and domain databases

InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR001621. Ligninase.
IPR024589. Ligninase_C.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF11895. DUF3415. 1 hit.
PF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00462. LIGNINASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLIG6_PHACH
AccessioniPrimary (citable) accession number: P50622
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 7, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.